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Analysis of heat shock‐induced monophosphorylation of stathmin in human T lymphoblastic cell line JURKAT by two‐dimensional gel electrophoresis
Author(s) -
Fujimoto Masanori,
Nagasaka Yuji,
Tanaka Tatehiko,
Nakamura Kazuyuki
Publication year - 1998
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150191426
Subject(s) - stathmin , jurkat cells , isoelectric point , heat shock protein , protein kinase a , microbiology and biotechnology , staurosporine , kinase , gel electrophoresis , isoelectric focusing , protein kinase c , biology , biochemistry , phosphorylation , enzyme , t cell , immunology , immune system , gene
Two‐dimensional gel electrophoresis (2‐DE) was used to study alterations in intracellular proteins of the human T lymphoblastic cell line JURKAT by heat shock at 45°C for 30 min. The 2‐DE patterns indicated an increase in the amount of a spot of molecular weight ( M r ) 18500 and isoelectric point (p I ) 5.6, which was a monophosphorylated form of stathmin. Stathmin is a major substrate for a proline‐rich peptide‐specific serine protein kinase, a mitogen‐activated protein kinase, however, the enzyme was not activated by the heat shock. Further examinations of the effects of cAMP, phorbol myristate acetate, cyclosporin A, and staurosporine on phosphorylation suggest that cyclin‐dependent kinases might be responsible for the heat shock‐induced monophosphorylation of stathmin.